|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
656-928 |
3.52e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 656 KQQEK---------ELFKLNQDNYI-----LQAKLSSFEET-NKKQRWLHFGEAADPVTGEKLKQIQKEIQEQETLLQGY 720
Cdd:TIGR02168 207 RQAEKaerykelkaELRELELALLVlrleeLREELEELQEElKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 721 QQENERLYNQVKDLQEQNKKNEERMfkenQSLFSEVASLKEQMHKSRflSQVVEDSEptrnqNFTDLLAELRMAQKEKDS 800
Cdd:TIGR02168 287 QKELYALANEISRLEQQKQILRERL----ANLERQLEELEAQLEELE--SKLDELAE-----ELAELEEKLEELKEELES 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 801 LLEDIKRLKQDKQALEVDFEKMKKERDQAKDQIAyVTGEKLYEIKILEETHKQEISRLQKRLQWYAENQELLDKDA--LR 878
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQLETLRSKVA-QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeeAE 434
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2462606921 879 LREANEEIEKLKLEIEKLKAESGNpSIRQKIRLKDKAADAK-KIQDLERQV 928
Cdd:TIGR02168 435 LKELQAELEELEEELEELQEELER-LEEALEELREELEEAEqALDAAEREL 484
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
657-897 |
3.83e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 657 QQEKELFKLNQDNYILQAKLSS-FEETNKKQRWLHFGEAADPVTGEKLKQIQKEIQEqetLLQGYQQENERLYNQVKDLQ 735
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSlQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ---LEQEEEKLKERLEELEEDLS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 736 --EQNKKNEERMFKENQSlfsEVASLKEQMHKSRFLSQVVEDSE-PTRNQNFTDLLAELRMAQKEKDSLLEDI----KRL 808
Cdd:TIGR02169 748 slEQEIENVKSELKELEA---RIEELEEDLHKLEEALNDLEARLsHSRIPEIQAELSKLEEEVSRIEARLREIeqklNRL 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 809 KQDKQALEVDFEKMKKERDQAKDQIAYVtGEKLYEIKILEETHKQEISRLQKRLQWYAENQELLDKDALR----LREANE 884
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSI-EKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEleaqLRELER 903
|
250
....*....|...
gi 2462606921 885 EIEKLKLEIEKLK 897
Cdd:TIGR02169 904 KIEELEAQIEKKR 916
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
668-894 |
5.61e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.48 E-value: 5.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 668 DNYILQAKLSSFEETNKKQRWLhfgeaadpvtGEKLKQIQKEIQEQETLLQGYQQENerlynQVKDLQEQNKKNEERMFK 747
Cdd:COG3206 159 EAYLEQNLELRREEARKALEFL----------EEQLPELRKELEEAEAALEEFRQKN-----GLVDLSEEAKLLLQQLSE 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 748 ENQSLFSEVASLKEQMHKSRFLSQVVEDSEPT-----RNQNFTDLLAELRMAQKEKDSLLE-------DIKRLKQDKQAL 815
Cdd:COG3206 224 LESQLAEARAELAEAEARLAALRAQLGSGPDAlpellQSPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAAL 303
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462606921 816 EvdfEKMKKERDQAKDQIayvtgeklyeikileethKQEISRLQKRLQWYAENQELLDKDALRLREANEEIEKLKLEIE 894
Cdd:COG3206 304 R---AQLQQEAQRILASL------------------EAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
701-928 |
1.00e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.75 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 701 EKLKQIQKEIQEQETLLQGYQQENERLYNQVKDLQeqnkkneermfKENQSLFSEVASLKEQMHKSRFLSQVVEDSEPTR 780
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLR-----------KELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 781 NQNFTDLLAELRMAQKEKDSLLEDIKRLKQDKQALEVDFEKMKKERDQAKDQIAYV------TGEKLYEIKILEETHKQE 854
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELraeltlLNEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462606921 855 ISRLQKRLQWYAE----NQELLDKDALRLREANEEIEKLKLEIEKLKAESGNPSIRQKIRLKDKAADAKKIQDLERQV 928
Cdd:TIGR02168 833 IAATERRLEDLEEqieeLSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
617-899 |
1.05e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 617 KRVQEAEDKWRGAQALIEQIKATfSEKEKELENKLEELKKQQEKELFKLNQDNYILQAKLssfEETNKKQRwlhfgeaad 696
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAE-LEELEAELEELEAELAELEAELEELRLELEELELEL---EEAQAEEY--------- 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 697 pVTGEKLKQIQKEIQEQETLLQGYQQENERLYNQVKDLQEQNKKNEERMfkenQSLFSEVASLKEQMHKSRFLSQVVEDS 776
Cdd:COG1196 292 -ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL----EELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 777 EPTRNQNFTDLLAELRMAQKEKDSLLEDIKRLKQDKQALEVDFEKMKKERDQAKDQIAyvtgEKLYEIKILEETHKQEIS 856
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE----ELEEALAELEEEEEEEEE 442
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2462606921 857 RLQKRLQWYAENQELLDKDALRLREANEEIEKLKLEIEKLKAE 899
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
700-902 |
8.46e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 8.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 700 GEKLKQIQKEIQEQETLLQGYQ-QENERLYNQVKDLQEQNKKneermfkenqslfsEVASLKEQMHKSRflsqvvedsep 778
Cdd:COG4913 261 AERYAAARERLAELEYLRAALRlWFAQRRLELLEAELEELRA--------------ELARLEAELERLE----------- 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 779 trnQNFTDLLAELRMAQKEKDSL-LEDIKRLKQDKQALEVDFEKMKKERDQAKDQIAYVTGEKLYEIKILEETHKQEISR 857
Cdd:COG4913 316 ---ARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAAL 392
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462606921 858 LQKRLQWYAENQELLDKDALRLREANEEIEKLKLEIEKLKAESGN 902
Cdd:COG4913 393 LEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSN 437
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
613-911 |
1.14e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 613 LLMFKRVQEAEDKWRGAQALIEQIKAtfsekekelenkleeLKKQQEKELFKLNQDnyilqaklssfEETNKKQrwlhfg 692
Cdd:COG4942 9 LLLALAAAAQADAAAEAEAELEQLQQ---------------EIAELEKELAALKKE-----------EKALLKQ------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 693 eaadpvtgekLKQIQKEIQEQETLLQGYQQENERLYNQVKDLQEQNKKNEERMfKENQSLFSEVASLKEQMHKSRFLSQV 772
Cdd:COG4942 57 ----------LAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL-EAQKEELAELLRALYRLGRQPPLALL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 773 VEDSEPTRNQNFTDLLAELRMAQKEkdsLLEDIKRLKQDKQALEVDFEKMKKERDQAKDQIAyvtgEKLYEIKILEETHK 852
Cdd:COG4942 126 LSPEDFLDAVRRLQYLKYLAPARRE---QAEELRADLAELAALRAELEAERAELEALLAELE----EERAALEALKAERQ 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462606921 853 QEISRLQKRLQWYAENQELLDKDALRLREANEEIEKLKLEIEKLKAESGNPSIRQKIRL 911
Cdd:COG4942 199 KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLPW 257
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
611-899 |
1.76e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.91 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 611 KKLLMFKRVQEAEDKWRGAQALIEQIKATFSEKEKElENKLEELKKQQEKELFKLNQDNYI-LQAKLSSFEetnkkqrwl 689
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKR-LEEIEQLLEELNKKIKDLGEEEQLrVKEKIGELE--------- 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 690 hfgeaadpVTGEKLKQIQKEIQEQETLLQGYQQENERLYNQVKDLQEQNKKNEERMFKENQSLFSEVASLKEQMHKSRFL 769
Cdd:TIGR02169 301 --------AEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 770 SQVVEDSEPTRNQNFTDLLAELRMAQKEKDSLLEDIKRLKQDKQALEVDFEKMKKERDQAKDQIAYVTGEKlyEIKILE- 848
Cdd:TIGR02169 373 LEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK--EDKALEi 450
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2462606921 849 ETHKQEISRLQKRLQwyAENQELLDKDAlRLREANEEIEKLKLEIEKLKAE 899
Cdd:TIGR02169 451 KKQEWKLEQLAADLS--KYEQELYDLKE-EYDRVEKELSKLQRELAEAEAQ 498
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
701-910 |
2.13e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 701 EKLKQIQKEIQEQETLLQGYQQENERLYNQVKDLQEQNKKNEErMFKENQSLFSEVASLKEQMHKSRFLSQVVEDSEPTR 780
Cdd:PRK03918 518 EELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAE-LEKKLDELEEELAELLKELEELGFESVEELEERLKE 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 781 NQNFTDLLAELRMAQKEKDSLLEDIKRLKQDKQALEVDFEKMKKERDQAKDQIAYV----TGEKLYEIKILEETHKQEIS 856
Cdd:PRK03918 597 LEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELekkySEEEYEELREEYLELSRELA 676
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462606921 857 RLQKRLQWYAENQELLDKDALRLREANEEIEKLKLEIEKL-KAESGNPSIRQKIR 910
Cdd:PRK03918 677 GLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLeKALERVEELREKVK 731
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
701-862 |
2.36e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 701 EKLKQIQKEIQEQETLLQGYQQENERLYNQVKDLQEQNKKNEErmfkenqslfsEVASLKEQMHKSRFLSQVVEDseptr 780
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLEL-----------EIEEVEARIKKYEEQLGNVRN----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 781 NQNFTDLLAELRMAQKEKDSLLEDIKRLKQDKQALEVDFEKMKKERDQAKDQIAYVTGE---KLYEIKILEETHKQEISR 857
Cdd:COG1579 88 NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEldeELAELEAELEELEAEREE 167
|
....*
gi 2462606921 858 LQKRL 862
Cdd:COG1579 168 LAAKI 172
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
696-927 |
2.44e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 696 DPVTGEKLKQIQKEIQEqetlLQGYQQENERLYNQVKDLQEQNKKNEERmfkenQSLFSEVASLKEQMHKSRFLsqvved 775
Cdd:COG4913 220 EPDTFEAADALVEHFDD----LERAHEALEDAREQIELLEPIRELAERY-----AAARERLAELEYLRAALRLW------ 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 776 septRNQNFTDLLaelrmaQKEKDSLLEDIKRLKQDKQALEVDFEKMKKERDQAKDQIAYVTGEKLYEIKILEETHKQEI 855
Cdd:COG4913 285 ----FAQRRLELL------EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLEREL 354
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462606921 856 SRLQKRLQWYaenQELLDKDALRLREANEEIEKLKLEIEKLKAESGnpsiRQKIRLKDKAADAK-KIQDLERQ 927
Cdd:COG4913 355 EERERRRARL---EALLAALGLPLPASAEEFAALRAEAAALLEALE----EELEALEEALAEAEaALRDLRRE 420
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
695-889 |
3.83e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 695 ADPVTG----EKLKQIQKEIQEQETLLQGYQQENERLYNQVKDLQEQnkKNEERMFKENQSLFSEVASLKEQMH-KSRFL 769
Cdd:COG4913 600 SRYVLGfdnrAKLAALEAELAELEEELAEAEERLEALEAELDALQER--REALQRLAEYSWDEIDVASAEREIAeLEAEL 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 770 SQVVEDseptrNQNFTDLLAELRMAQKEKDSLLEDIKRLKQDKQALEVDFEKMKKERDQAKDQI-AYVTGEKLYEIKILE 848
Cdd:COG4913 678 ERLDAS-----SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLeAAEDLARLELRALLE 752
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2462606921 849 ETHKQEI-SRLQKRL-QWYAENQELLDKdalRLREANEEIEKL 889
Cdd:COG4913 753 ERFAAALgDAVERELrENLEERIDALRA---RLNRAEEELERA 792
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
695-904 |
4.41e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 695 ADP---VTGEKLKQIQKEIQEQETLLQGYQQENERLYNQVKDLQEQNKKNEERM-------------FKENQSLFSEVA- 757
Cdd:COG3883 14 ADPqiqAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIdklqaeiaeaeaeIEERREELGERAr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 758 SLKEQMHKSRFLSQVVEdseptrNQNFTDLLAELRMAQKEKDSLLEDIKRLKQDKQALEVDFEKMKKERDQAKDQIAYVt 837
Cdd:COG3883 94 ALYRSGGSVSYLDVLLG------SESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL- 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462606921 838 geklyeikileETHKQEISRLQkrlqwyAENQELLDKDALRLREANEEIEKLKLEIEKLKAESGNPS 904
Cdd:COG3883 167 -----------EAAKAELEAQQ------AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
607-899 |
5.30e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 5.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 607 ENKEKKLLMFKRVQEAEDKWRGAQALIEQIKATFSEKekelenkleelkkqqEKELFKLNQDNYILQAKLSSFEETNKKQ 686
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSEL---------------EEEIEELQKELYALANEISRLEQQKQIL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 687 RwlhfgeaadpvtgEKLKQIQKEIQEQETLLQGYQQENERLynqvkdlqeqnKKNEERMFKENQSLFSEVASLKEQMHKS 766
Cdd:TIGR02168 308 R-------------ERLANLERQLEELEAQLEELESKLDEL-----------AEELAELEEKLEELKEELESLEAELEEL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 767 RFLSQVVEDSEPTRNQNFTDLLAELRMAQKEKDSLLEDIKRLKQDKQALEVDFEKMKKERDQAKDQIAYVtgeKLYEIKI 846
Cdd:TIGR02168 364 EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA---ELKELQA 440
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2462606921 847 LEETHKQEISRLQKRLQWYAENQELLDKdalRLREANEEIEKLKLEIEKLKAE 899
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELRE---ELEEAEQALDAAERELAQLQAR 490
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
656-899 |
5.44e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 5.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 656 KQQEKELFKLNQDNYILQaklssfEETNKKQRWLHFGEAADPVTGEKLKQIQKEIQEQETLLQGYQQENERLYNQVKDLQ 735
Cdd:TIGR02168 694 AELEKALAELRKELEELE------EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 736 EQNKKNEE---RMFKENQSLFSEVASLKEQMHKSRFLSQVVEDSEPTRNQNFTDLLAELRMAQKEKDSLLEDIKRLKQDK 812
Cdd:TIGR02168 768 ERLEEAEEelaEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 813 QALEVDFEKMKKERDQAKDQIAYVTgEKLYEIKILEETHKQEISRLQKRLQWYAENQELLDKDALRLR----EANEEIEK 888
Cdd:TIGR02168 848 EELSEDIESLAAEIEELEELIEELE-SELEALLNERASLEEALALLRSELEELSEELRELESKRSELRreleELREKLAQ 926
|
250
....*....|.
gi 2462606921 889 LKLEIEKLKAE 899
Cdd:TIGR02168 927 LELRLEGLEVR 937
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
701-919 |
9.11e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 9.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 701 EKLKQIQKEIQEQETLLQGYQQE----NERLYNQVKDLQEQNKKNEERMFKENQSLFSEVASLKEQMHKsrflsqvVEDS 776
Cdd:TIGR02169 237 RQKEAIERQLASLEEELEKLTEEiselEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIAS-------LERS 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 777 EPTRNQNFTDLLAELRMAQKEKDSLLEDIkrlkqdkQALEVDFEKMKKERDQAKDqiayvtgeklyEIKILEETHKQEIS 856
Cdd:TIGR02169 310 IAEKERELEDAEERLAKLEAEIDKLLAEI-------EELEREIEEERKRRDKLTE-----------EYAELKEELEDLRA 371
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462606921 857 RLQKRLQWYAENQELLDKDALRLREANEEIEKLKLEIEKLKAESGNPSIRQKiRLKDKAADAK 919
Cdd:TIGR02169 372 ELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELA-DLNAAIAGIE 433
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
786-928 |
1.50e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 786 DLLAELRMAQKEKDSLLEDIKRLKQDKQALEvdfekmkkERDQAKDQIAYVTGEklyEIKIleETHKQEISRLQKRLqwy 865
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQ--------ERREALQRLAEYSWD---EIDV--ASAEREIAELEAEL--- 677
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462606921 866 aenqELLDKDALRLREANEEIEKLKLEIEKLKAESGNpSIRQKIRLKDKAADAKK-IQDLERQV 928
Cdd:COG4913 678 ----ERLDASSDDLAALEEQLEELEAELEELEEELDE-LKGEIGRLEKELEQAEEeLDELQDRL 736
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
788-928 |
3.50e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 788 LAELRMAQKEKDSLLEDIKRLKQDKQALEVDFEKMKKERDQAKDQIayvtgeKLYEIKILEETHKQEISRLQKRLQWYAE 867
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREEL------EKLEKLLQLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462606921 868 NQELLDKDALRLREANEEIEKLKLEIEKLKAEsgnpsiRQKIRLKDKAADAKKIQDLERQV 928
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEE------LEELLEQLSLATEEELQDLAEEL 201
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
701-899 |
3.78e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 701 EKLKQIQKEIQEQETLLQGYQQENErlynQVKDLQEQNKKNEERMFKENQSLFSEVASLKEQMHKsrfLSQVVEDSEPTR 780
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTE----NIEELIKEKEKELEEVLREINEISSELPELREELEK---LEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 781 NqnftdllaELRMAQKEKDSLLEDIKRLKQDKQALEVDFEKMKKERDQAKDQIAYVT-----GEKLYEIKILEETHKQEI 855
Cdd:PRK03918 238 E--------EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKelkekAEEYIKLSEFYEEYLDEL 309
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462606921 856 SRLQKRLQWYAENQELLDKDALRLREANEEIEKLKLEIEKLKAE 899
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKR 353
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
786-898 |
4.41e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.08 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 786 DLLAELRMAQKEKDSLLEDIKRLKQDKQALEvdfEKMKKERDQAKDQIayvtgEKLYEIKILEEthkqEISRLQKRLqwy 865
Cdd:COG2433 417 RLEEQVERLEAEVEELEAELEEKDERIERLE---RELSEARSEERREI-----RKDREISRLDR----EIERLEREL--- 481
|
90 100 110
....*....|....*....|....*....|...
gi 2462606921 866 aenqelldkdalrlREANEEIEKLKLEIEKLKA 898
Cdd:COG2433 482 --------------EEERERIEELKRKLERLKE 500
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
784-927 |
4.56e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 784 FTDLLAELRMAQKEKDSLLEDIKRLKQDKQALEVDFEKMKKE-------RDQAKDQIAYVTGEKLYEIKILEETHKQEIS 856
Cdd:TIGR02169 225 GYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRleeieqlLEELNKKIKDLGEEEQLRVKEKIGELEAEIA 304
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462606921 857 RLQKRLQWYAENQELLDKdalRLREANEEIEKLKLEIEKLKAESGNPSIRqKIRLKDKAADAKKIQDLERQ 927
Cdd:TIGR02169 305 SLERSIAEKERELEDAEE---RLAKLEAEIDKLLAEIEELEREIEEERKR-RDKLTEEYAELKEELEDLRA 371
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
789-899 |
4.65e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 789 AELRMAQKEKDSLLEDIKR----LKQDKQaLEVDfEKMKKERDQAKDQIAyvtgEKLYEIKILEETHKQEISRLQKRLQW 864
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKeaeaIKKEAL-LEAK-EEIHKLRNEFEKELR----ERRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110
....*....|....*....|....*....|....*
gi 2462606921 865 YAENQELLDKDALRLREANEEIEKLKLEIEKLKAE 899
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIEE 139
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
653-928 |
5.01e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 653 ELKKQQEK-ELFKLNQDNY-ILQAKLSSFEETNKKQRWLHFGEAADpVTGEKLKQIQKEIQEQETLLQGYQQENERLYNQ 730
Cdd:COG1196 204 PLERQAEKaERYRELKEELkELEAELLLLKLRELEAELEELEAELE-ELEAELEELEAELAELEAELEELRLELEELELE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 731 VKDLQ----------EQNKKNEERMFKENQSLFSEVASLKEQMHKSRFLSQVVEDSEPTRNQNFTDLLAELRMAQKEKDS 800
Cdd:COG1196 283 LEEAQaeeyellaelARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 801 LLEDIKRLKQDKQALEVDFEKMKKERDQAKDQIAyvtgEKLYEIKILEETHKQEISRLQKRLQWYAENQELLDKDALRLR 880
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAA----ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2462606921 881 EANEEIEKLKLEIEKLKAESGNPSIRQKIRLKDKAADAKKIQDLERQV 928
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
699-891 |
1.63e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 699 TGEKLKQIQKEIQEQETLLQGYQQENERLYNQVKDLQEQNKKneermFKENQSLFSEVASLKEQMHKSRFLSQVVEDSEP 778
Cdd:COG4717 62 QGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEE-----LEELEAELEELREELEKLEKLLQLLPLYQELEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 779 TRNQ--NFTDLLAELRMAQKEKDSLLEDIKRLKQDKQALEVDFEKMKKERDQAKDQIAYVTGEKLYEIKILEETHKQEIS 856
Cdd:COG4717 137 LEAElaELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE 216
|
170 180 190
....*....|....*....|....*....|....*
gi 2462606921 857 RLQKRLQWYAENQELLDKDALRLrEANEEIEKLKL 891
Cdd:COG4717 217 EAQEELEELEEELEQLENELEAA-ALEERLKEARL 250
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
701-899 |
1.71e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 701 EKLKQIQKEIQEQETLLQGYQQENERLYNQVKDLQEQNKKNeermFKENQSLFSEVASLKEQMHKSRFLSQVVEDSEPTR 780
Cdd:TIGR04523 342 EQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY----KQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 781 NQNFTDLLAELRMAQKEKDSLLEDIKRLKQDKQALEVDFEKMKKERDQAKDQIAYVTGEKLYEIKILEETHKQEISRLQK 860
Cdd:TIGR04523 418 QQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE 497
|
170 180 190
....*....|....*....|....*....|....*....
gi 2462606921 861 RLQWYAENQELLDKdalrLREANEEIEKLKLEIEKLKAE 899
Cdd:TIGR04523 498 LKKLNEEKKELEEK----VKDLTKKISSLKEKIEKLESE 532
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
657-863 |
2.21e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 657 QQEKELFKLNQDNYILQAKLSSFEETNKKQRWLHFGEAAdpvtgEKLKQIQKEIQEQET--LLQGYQQENERLYNQ--VK 732
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRI-----EELQELLREAEELEEelQLEELEQEIAALLAEagVE 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 733 DLQEQNKKNEErmFKENQSLFSEVASLKEQM--HKSRFLSQVVEDSEPTRNQNFTDLLAELRMAQKEKDSLLEDIKRLKQ 810
Cdd:COG4717 383 DEEELRAALEQ--AEEYQELKEELEELEEQLeeLLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEA 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462606921 811 DKQALEVD--FEKMKKERDQAKDQIAYVTgEKLYEIKILEETHKQEISRLQKRLQ 863
Cdd:COG4717 461 ELEQLEEDgeLAELLQELEELKAELRELA-EEWAALKLALELLEEAREEYREERL 514
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
710-931 |
2.88e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.26 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 710 IQEQETLLQGYQQENERLYNQVKDLQEQNKKNEERMFKENQSLfSEVASLKEQMHKSRFLSQVVEDSEPTRNqnftdlLA 789
Cdd:pfam17380 377 MRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQK-VEMEQIRAEQEEARQREVRRLEEERARE------ME 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 790 ELRMAQKEKDSLLEDIKRLKQDKQALEVDFEKMKKERDQAKDQIAYVTGEKLYEIK--ILEETHKQEIsrLQKRLQwyaE 867
Cdd:pfam17380 450 RVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKqaMIEEERKRKL--LEKEME---E 524
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462606921 868 NQELLDKDALRlREANEEIEKlKLEIEKLKaesgnpSIRQKIRLKDKAADAKKIQDLERQVCVQ 931
Cdd:pfam17380 525 RQKAIYEEERR-REAEEERRK-QQEMEERR------RIQEQMRKATEERSRLEAMEREREMMRQ 580
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
700-825 |
3.44e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 700 GEKLKQIQKEIQEQETLLQGYQQENERLYNQVKDLQEQNKKNEERmFKENQSlfsEVASLKEQMHKSRFLSQvvedsept 779
Cdd:COG4913 337 GDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE-FAALRA---EAAALLEALEEELEALE-------- 404
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2462606921 780 rnQNFTDLLAELRMAQKEKDSLLEDIKRLKQDKQALEVDFEKMKKE 825
Cdd:COG4913 405 --EALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDA 448
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
786-899 |
3.59e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 786 DLLAELRMAQKEKDSLLEDIKRLKQDKQALEVDFEKMKKERDQAKDQIAYVTGEKLYEIKILE-ETHKQEISRLQKRLQw 864
Cdd:COG1579 35 ELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQKEiESLKRRISDLEDEIL- 113
|
90 100 110
....*....|....*....|....*....|....*
gi 2462606921 865 yaENQELLDKDALRLREANEEIEKLKLEIEKLKAE 899
Cdd:COG1579 114 --ELMERIEELEEELAELEAELAELEAELEEKKAE 146
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
707-899 |
6.03e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.30 E-value: 6.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 707 QKEIQEQETLLQGYQQENERLYNQVKDLQEQNKKNEERMFKENQSLFSEVASLKEqmhksRFLSQVVEDseptrnqnFTD 786
Cdd:PRK05771 38 EELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVE-----EELEKIEKE--------IKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 787 LLAELRMAQKEKDSLLEDIKRLKQDKqALEVDFEKMKKER-----------DQAKDQIAYVTGEKLYEIKILEET----- 850
Cdd:PRK05771 105 LEEEISELENEIKELEQEIERLEPWG-NFDLDLSLLLGFKyvsvfvgtvpeDKLEELKLESDVENVEYISTDKGYvyvvv 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462606921 851 -----HKQEISRLQKRLQWYAEN-------QELLDKDALRLREANEEIEKLKLEIEKLKAE 899
Cdd:PRK05771 184 vvlkeLSDEVEEELKKLGFERLEleeegtpSELIREIKEELEEIEKERESLLEELKELAKK 244
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
711-826 |
7.26e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 39.88 E-value: 7.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 711 QEQETLLQGYQQENERLYNQVKDLQEQNKK-NEERMfkENQSLFSEVASLKEqmhksrflSQVVEDSEPTRNqnFTDLLA 789
Cdd:pfam07888 304 QERETLQQSAEADKDRIEKLSAELQRLEERlQEERM--EREKLEVELGREKD--------CNRVQLSESRRE--LQELKA 371
|
90 100 110
....*....|....*....|....*....|....*..
gi 2462606921 790 ELRMAQKEKDSLLEDIKRLKQDKQALEVDFEKMKKER 826
Cdd:pfam07888 372 SLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVADAK 408
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
701-881 |
8.40e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 39.88 E-value: 8.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 701 EKLKQIQKEIQEQETLLQGYQQENERLYNQVKDLQEQNKKNEERMfkenQSLFSEVASLKEQMHKSRFLSQVVEDSEPTR 780
Cdd:pfam07888 38 ECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRV----AELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 781 NQNFTDLLAELRMAQKEKDSLLEDIKRLKQDKQALEVDFEKMKKERDQAKDQIAYVTGEKLYEIKILEEThKQEISRLQK 860
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQT-EEELRSLSK 192
|
170 180
....*....|....*....|.
gi 2462606921 861 RLQWYAENQELLDKDALRLRE 881
Cdd:pfam07888 193 EFQELRNSLAQRDTQVLQLQD 213
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
617-889 |
8.65e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.05 E-value: 8.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 617 KRVQEAEDKWRGAQALIEQIKATFSEKEKELENKLEELKKqQEKELFKLNQDNYILQAKLSSFEETNKKQRWLHFGEAAD 696
Cdd:TIGR02169 723 KEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKE-LEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELS 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 697 PVTgEKLKQIQKEIQEQETLLQGYQQENERLYNQVKDLQEQNKKNEERMfkenQSLFSEVASLKEQMHKsrfLSQVVEDS 776
Cdd:TIGR02169 802 KLE-EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI----KSIEKEIENLNGKKEE---LEEELEEL 873
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606921 777 EptrnqnftdllAELRMAQKEKDSLLEDIKRLKQDKQALEVDFEKMKKERDQAKDQIayvtGEKLYEIKILEETHKqEIS 856
Cdd:TIGR02169 874 E-----------AALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRL----SELKAKLEALEEELS-EIE 937
|
250 260 270
....*....|....*....|....*....|...
gi 2462606921 857 RLQKRLQWYAENQELLDKDALRLREANEEIEKL 889
Cdd:TIGR02169 938 DPKGEDEEIPEEELSLEDVQAELQRVEEEIRAL 970
|
|
|